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Ureaplasma urealyticum urease genes; use of a UGA tryptophan codon
Author(s) -
Blanchard A.
Publication year - 1990
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.1990.tb00636.x
Subject(s) - biology , ureaplasma urealyticum , gene , homology (biology) , genetics , open reading frame , nucleic acid sequence , canavalia ensiformis , urease , stop codon , polymerase chain reaction , biochemistry , peptide sequence , microbiology and biotechnology , enzyme , mycoplasma
Summary Nucleotide sequence analysis of a Ureaplasma urealyticum DNA fragment, homologous to cloned urease genes of other prokaryotes, revealed three consecutive open reading frames. The molecular weights of the three deduced polypeptides are 11.2kD, 13.6kD and 66.6 kD. These values are consistent with the size of the three subunits previously reported for purified native urease. A significant sequence homology was found between the three polypeptides of the ureaplasmal urease and the single polypeptide of jack bean ( Canavalia ensiformis ) urease. Codon usage indicates that UGA is a tryptophan codon in this mollicute. Use of polymerase chain reactions has disclosed the existence of genetic polymorphism among the urease genes of different serotypes of U. urealyticum.